ArticleJournal of the American Chemical Society2015
Electrocatalytic O2-Reduction by Synthetic Cytochrome c Oxidase Mimics: Identification of a "Bridging Peroxo" Intermediate Involved in Facile 4e(-)/4H(+) O2-Reduction.
Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 109 citations in OpenAlex.
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- A Minimalist Iron Porphyrin Which Can Catalyze Both Peroxidation and Oxygen Reduction Reaction.JACS Au · 2025Article
- A Bioinspired Nonheme FeJournal of the American Chemical Society · 2024Article
- Heme-copper and Heme OJournal of inorganic biochemistry · 2023Review
- Review
- Proton-coupled electron transfer reactivities of electronically divergent heme superoxide intermediates: a kinetic, thermodynamic, and theoretical study.Chemical science · 2021Article
- Molecular understanding of heteronuclear active sites in heme-copper oxidases, nitric oxide reductases, and sulfite reductases through biomimetic modelling.Chemical Society reviews · 2021Review
- Structural Determination of an Unusual CuChemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Significantly improved electrocatalytic oxygen reduction by an asymmetrical Pacman dinuclear cobalt(ii) porphyrin-porphyrin dyad.Chemical science · 2020Article
- Heme-Cu Binucleating Ligand Supports Heme/OInorganic chemistry · 2019Article
- Influence of the distal guanidine group on the rate and selectivity of OChemical science · 2019Article
- Elucidation of the Structure of a Thiol Functionalized Cu-tmpa Complex Anchored to Gold via a Self-Assembled Monolayer.Inorganic chemistry · 2019Article
- Electrocatalytic hydrogen evolution with gallium hydride and ligand-centered reduction.Chemical science · 2019Article
- Synthetic Fe/Cu Complexes: Toward Understanding Heme-Copper Oxidase Structure and Function.Chemical reviews · 2018Review
- OACS catalysis · 2018Article
- Oxygen Activation and Energy Conservation by Cytochrome c Oxidase.Chemical reviews · 2018Review
- A water-soluble supramolecular complex that mimics the heme/copper hetero-binuclear site of cytochromeChemical science · 2018Article
- Activation of dioxygen by copper metalloproteins and insights from model complexes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Review
- Copper-Oxygen Complexes Revisited: Structures, Spectroscopy, and Reactivity.Chemical reviews · 2017Review
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
A synthetic heme-Cu CcO model complex shows selective and highly efficient electrocatalytic 4e(-)/4H(+) O2-reduction to H2O with a large catalytic rate (>10(5) M(-1) s(-1)). While the heme-Cu model (FeCu) shows almost exclusive 4e(-)/4H(+) reduction of O2 to H2O (detected using ring disk electrochemistry and rotating ring disk electrochemistry), when imidazole is bound to the heme (Fe(Im)Cu), this same selective O2-reduction to water occurs only under slow electron fluxes. Surface enhanced resonance Raman spectroscopy coupled to dynamic electrochemistry data suggests the formation of a bridging peroxide intermediate during O2-reduction by both complexes under steady state reaction conditions, indicating that O-O bond heterolysis is likely to be the rate-determining step (RDS) at the mass transfer limited region. The O-O vibrational frequencies at 819 cm(-1) in (16)O2 (759 cm(-1) in (18)O2) for the FeCu complex and at 847 cm(-1) (786 cm(-1)) for the Fe(Im)Cu complex, indicate the formation of side-on and end-on bridging Fe-peroxo-Cu intermediates, respectively, during O2-reduction in an aqueous environment. These data suggest that side-on bridging peroxide intermediates are involved in fast and selective O2-reduction in these synthetic complexes. The greater amount of H2O2 production by the imidazole bound complex under fast electron transfer is due to 1e(-)/1H(+) O2-reduction by the distal Cu where O2 binding to the water bound low spin Fe(II) complex is inhibited.
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